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Copper in PDB 5z62: Structure of Human Cytochrome C Oxidase

Enzymatic activity of Structure of Human Cytochrome C Oxidase

All present enzymatic activity of Structure of Human Cytochrome C Oxidase:
1.9.3.1;

Other elements in 5z62:

The structure of Structure of Human Cytochrome C Oxidase also contains other interesting chemical elements:

Magnesium (Mg) 1 atom
Zinc (Zn) 1 atom
Iron (Fe) 2 atoms

Copper Binding Sites:

The binding sites of Copper atom in the Structure of Human Cytochrome C Oxidase (pdb code 5z62). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 3 binding sites of Copper where determined in the Structure of Human Cytochrome C Oxidase, PDB code: 5z62:
Jump to Copper binding site number: 1; 2; 3;

Copper binding site 1 out of 3 in 5z62

Go back to Copper Binding Sites List in 5z62
Copper binding site 1 out of 3 in the Structure of Human Cytochrome C Oxidase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Structure of Human Cytochrome C Oxidase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu601

b:65.3
occ:1.00
ND1 A:HIS240 2.1 62.3 1.0
NE2 A:HIS291 2.1 58.3 1.0
NE2 A:HIS290 2.1 62.2 1.0
CE1 A:HIS240 2.8 62.3 1.0
CE1 A:HIS291 3.0 58.3 1.0
CE1 A:HIS290 3.0 62.2 1.0
CG A:HIS240 3.1 62.3 1.0
CD2 A:HIS291 3.1 58.3 1.0
CD2 A:HIS290 3.1 62.2 1.0
CB A:HIS240 3.6 62.3 1.0
NE2 A:HIS240 3.8 62.3 1.0
CD2 A:HIS240 4.0 62.3 1.0
ND1 A:HIS291 4.1 58.3 1.0
ND1 A:HIS290 4.1 62.2 1.0
CG A:HIS291 4.2 58.3 1.0
CA A:HIS240 4.2 62.3 1.0
CG A:HIS290 4.2 62.2 1.0
FE A:HEA604 4.5 58.4 1.0
C1A A:HEA604 4.6 58.4 1.0
ND A:HEA604 4.7 58.4 1.0
NA A:HEA604 4.8 58.4 1.0
C2A A:HEA604 4.8 58.4 1.0
C4A A:HEA604 4.9 58.4 1.0
C4D A:HEA604 4.9 58.4 1.0
CG2 A:VAL243 5.0 57.0 1.0
CHA A:HEA604 5.0 58.4 1.0
C3A A:HEA604 5.0 58.4 1.0
N A:HIS240 5.0 62.3 1.0

Copper binding site 2 out of 3 in 5z62

Go back to Copper Binding Sites List in 5z62
Copper binding site 2 out of 3 in the Structure of Human Cytochrome C Oxidase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Structure of Human Cytochrome C Oxidase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu301

b:0.0
occ:1.00
CU B:CU302 1.2 0.2 1.0
ND1 B:HIS161 2.2 70.6 1.0
SG B:CYS200 2.4 71.6 1.0
SG B:CYS196 2.4 74.2 1.0
CE1 B:HIS161 2.9 70.6 1.0
SD B:MET207 2.9 72.4 1.0
CB B:CYS200 3.2 71.6 1.0
CG B:HIS161 3.3 70.6 1.0
O B:GLU198 3.5 71.1 1.0
CE B:MET207 3.5 72.4 1.0
CB B:CYS196 3.6 74.2 1.0
ND1 B:HIS204 3.7 67.5 1.0
CB B:HIS161 3.9 70.6 1.0
CA B:HIS161 4.1 70.6 1.0
NE2 B:HIS161 4.1 70.6 1.0
CG B:MET207 4.1 72.4 1.0
CE1 B:HIS204 4.3 67.5 1.0
CD2 B:HIS161 4.3 70.6 1.0
O B:LEU160 4.5 70.5 1.0
CA B:CYS200 4.5 71.6 1.0
N B:CYS200 4.6 71.6 1.0
C B:GLU198 4.7 71.1 1.0
CG B:HIS204 4.9 67.5 1.0
CA B:HIS204 5.0 67.5 1.0

Copper binding site 3 out of 3 in 5z62

Go back to Copper Binding Sites List in 5z62
Copper binding site 3 out of 3 in the Structure of Human Cytochrome C Oxidase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Structure of Human Cytochrome C Oxidase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu302

b:0.2
occ:1.00
CU B:CU301 1.2 0.0 1.0
SG B:CYS200 2.4 71.6 1.0
SG B:CYS196 2.4 74.2 1.0
SD B:MET207 2.5 72.4 1.0
ND1 B:HIS204 3.0 67.5 1.0
CB B:CYS196 3.0 74.2 1.0
CG B:MET207 3.3 72.4 1.0
ND1 B:HIS161 3.3 70.6 1.0
CE B:MET207 3.5 72.4 1.0
CB B:CYS200 3.7 71.6 1.0
CE1 B:HIS204 3.7 67.5 1.0
CE1 B:HIS161 3.8 70.6 1.0
O B:HIS204 3.8 67.5 1.0
O B:GLU198 3.9 71.1 1.0
CA B:HIS204 4.0 67.5 1.0
CG B:HIS204 4.1 67.5 1.0
CB B:HIS204 4.4 67.5 1.0
C B:HIS204 4.4 67.5 1.0
CG B:HIS161 4.5 70.6 1.0
CA B:CYS196 4.5 74.2 1.0
N B:CYS200 4.7 71.6 1.0
CB B:MET207 4.7 72.4 1.0
CA B:CYS200 4.8 71.6 1.0
O B:ASN203 4.9 70.3 1.0
NE2 B:HIS204 5.0 67.5 1.0
CB B:HIS161 5.0 70.6 1.0

Reference:

S.Zong, M.Wu, J.Gu, T.Liu, R.Guo, M.Yang. Structure of the Intact 14-Subunit Human Cytochrome C Oxidase. Cell Res. V. 28 1026 2018.
ISSN: ISSN 1748-7838
PubMed: 30030519
DOI: 10.1038/S41422-018-0071-1
Page generated: Mon Jul 14 05:42:42 2025

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